Premium
Ecdysteroid‐stimulated synthesis and secretion of an N‐acetyl‐D‐glucosamine‐rich glycopeptide in a lepidopterna cell line derived from imaginal discs
Author(s) -
Porcheron Patrick,
Morinière Madeleine,
Coudouel Noëlline,
Oberlander Herbert
Publication year - 1991
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940160405
Subject(s) - biology , glucosamine , glycopeptide , cycloheximide , tunicamycin , ecdysteroid , biochemistry , secretion , glycoprotein , cell culture , ecdysone , chitin , imaginal disc , protein biosynthesis , hormone , drosophila melanogaster , genetics , unfolded protein response , endoplasmic reticulum , chitosan , gene , antibiotics
Hormone‐regulated processing of N‐acetyl‐D‐glucosamine was studied in an insect cell line derived from imaginal wing discs of the Indian meal moth, Plodia interpunctella (Hübner). The cell line, IAL‐PID2, responded to treatment with 20‐hydroxyecdysone with increased incorporation of GlcNAc into glycoproteins. Cycloheximide and tunicamycin counteracted the action of the hormone. In particular, treatment with 20‐hydroxyecdysone resulted in the secretion of a 5,000 dalton N‐acetyl‐D‐glucosamine‐rich glycopeptide by the IAL‐PID2 cells. Accumulation of this peptide was prevented by the use of teflubenzuron, a potent chitin synthesis inhibitor. A glycopeptide of similar molecular weight was observed in imaginal discs of P. interpunctella treated with 20‐hydroxyecdysone in vitro, under conditions that induce chitin synthesis. Although the function of the 5,000 dalton glycopeptide is not known, we believe that the PID2 cell line is a promising model for molecular analysis of ecdysteroid‐regulated processing of aminosugars by epidermal cells during insect development.